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6mud

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'''Unreleased structure'''
 
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The entry 6mud is ON HOLD
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==Voltage-gated sodium channel NaV1.5 C-terminal domain in complex with Ca2+/Calmodulin==
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<StructureSection load='6mud' size='340' side='right'caption='[[6mud]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MUD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mud OCA], [https://pdbe.org/6mud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mud RCSB], [https://www.ebi.ac.uk/pdbsum/6mud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mud ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_HUMAN] Catecholaminergic polymorphic ventricular tachycardia;Brugada syndrome;Romano-Ward syndrome. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM2 are the cause of LQT15.
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== Function ==
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[https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
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Authors:
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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Description:
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Gardill BR]]
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[[Category: Tung CC]]
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[[Category: Van Petegem F]]

Current revision

Voltage-gated sodium channel NaV1.5 C-terminal domain in complex with Ca2+/Calmodulin

PDB ID 6mud

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